Human calprotectin is an iron-sequestering host-defense protein. - Wikidata - awgldk - TriplyDB

Human calprotectin is an iron-sequestering host-defense protein.

Human calprotectin is an iron-sequestering host-defense protein.

http://www.wikidata.org/entity/Q43246197

about

Binding of transition metals to S100 proteins The Hexahistidine Motif of Host-Defense Protein Human Calprotectin Contributes to Zinc Withholding and Its Functional Versatility Transition metals at the host-pathogen interface: how Neisseria exploit human metalloproteins for acquiring iron and zinc.Antimicrobial peptides and wound healing: biological and therapeutic considerations Crystal structure of human S100A8 in complex with zinc and calcium.The Two-Component System ArlRS and Alterations in Metabolism Enable Staphylococcus aureus to Resist Calprotectin-Induced Manganese Starvation.A Superoxide Dismutase Capable of Functioning with Iron or Manganese Promotes the Resistance of Staphylococcus aureus to Calprotectin and Nutritional Immunity.The innate immune protein calprotectin promotes Pseudomonas aeruginosa and Staphylococcus aureus interaction.Acinetobacter baumannii Coordinates Urea Metabolism with Metal Import To Resist Host-Mediated Metal Limitation.Transition Metals and Virulence in Bacteria.A Pseudomonas T6SS effector recruits PQS-containing outer membrane vesicles for iron acquisition.Calcium Ions Tune the Zinc-Sequestering Properties and Antimicrobial Activity of Human S100A12.Calcium-induced Tetramerization and Zinc Chelation Shield Human Calprotectin from Degradation by Host and Bacterial Extracellular Proteases.An evaluation of calprotectin as serum marker of preeclampsia: a systematic review of observational studies.The Yin and Yang of copper during infection.Developmental Control of NRAMP1 (SLC11A1) Expression in Professional Phagocytes Iron Efflux by PmtA Is Critical for Oxidative Stress Resistance and Contributes Significantly to Group A Streptococcus Virulence.Bacterial Strategies to Maintain Zinc Metallostasis at the Host-Pathogen Interface.Competition for Iron Between Host and Pathogen: A Structural Case Study on Helicobacter pylori.Calprotectin in Daily Practice: Where Do We Stand in 2017?The Capacity of Mycobacterium tuberculosis To Survive Iron Starvation Might Enable It To Persist in Iron-Deprived Microenvironments of Human Granulomas.A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine Development.Nickel Sequestration by the Host-Defense Protein Human Calprotectin.Expression, Purification, and Antimicrobial Activity of S100A12.Fecal total iron concentration is inversely associated with fecal Lactobacillus in preschool children.Salmonella Mitigates Oxidative Stress and Thrives in the Inflamed Gut by Evading Calprotectin-Mediated Manganese Sequestration.Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin).The Metallophore Staphylopine Enables Staphylococcus aureus To Compete with the Host for Zinc and Overcome Nutritional Immunity.Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin.The role of calprotectin in withholding zinc and copper from Candida albicans.Metals: Calprotectin and iron match up.High Amounts of S100-Alarmins Confer Antimicrobial Activity on Human Breast Milk Targeting Pathogens Relevant in Neonatal Sepsis.Bioinorganic Explorations of Zn(II) Sequestration by Human S100 Host-Defense Proteins.G.I. pros: Antimicrobial defense in the gastrointestinal tract.Metals in fungal virulence.Human calprotectin affects the redox speciation of iron.Initial Biochemical and Functional Evaluation of Murine Calprotectin Reveals Ca(II)-Dependence and Its Ability to Chelate Multiple Nutrient Transition Metal Ions.Fecal calprotectin level in healthy children aged less than 4 years in South Korea.Calprotectin is a potential prognostic marker for polycystic ovary syndrome.

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P2860

Human calprotectin is an iron-sequestering host-defense protein.

http://www.wikidata.org/entity/Q43246197

description

2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年學術文章

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2015年學術文章

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name

Human calprotectin is an iron-sequestering host-defense protein.

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Human calprotectin is an iron-sequestering host-defense protein.

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type

label

Human calprotectin is an iron-sequestering host-defense protein.

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Human calprotectin is an iron-sequestering host-defense protein.

@nl

prefLabel

Human calprotectin is an iron-sequestering host-defense protein.

@en

Human calprotectin is an iron-sequestering host-defense protein.

@nl

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P1433

Nature Chemical Biology

P1476

Human calprotectin is an iron-sequestering host-defense protein.

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P2093

Bo Zhang

http://www.w3.org/2001/XMLSchema#string

Elizabeth M Nolan

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Toshiki G Nakashige

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P2860

Zinc-binding site of an S100 protein revealed. Two crystal structures of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free states

A component of innate immunity prevents bacterial biofilm development

Manganese and microbial pathogenesis: sequestration by the Mammalian immune system and utilization by microorganisms

The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EF-hand proteins

The crystal structures of human S100A12 in apo form and in complex with zinc: new insights into S100A12 oligomerisation

The crystal structures of human S100B in the zinc- and calcium-loaded state at three pH values reveal zinc ligand swapping

Molecular basis for manganese sequestration by calprotectin and roles in the innate immune response to invading bacterial pathogens

Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron

Feo--transport of ferrous iron into bacteria.

Biophysical characterization of S100A8 and S100A9 in the absence and presence of bivalent cations.

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765-771

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scholarly article

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10.1038/NCHEMBIO.1891

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10

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11

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2015-08-24T00:00:00Z

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26302479

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4575267

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